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Fig. 3. The ß-catenin destruction complex and its regulation by GBP and Dsh. (A) The destruction complex contains the large proteins Axin and APC, which bring ß-catenin (ß) into the complex and into close proximity to GSK3 and CK1{alpha}. These kinases phosphorylate (p) N-terminal residues in ß-catenin and target it for degradation by the ubiquitin-proteasome pathway. (B) GBP and Dishevelled (Dsh) cooperatively inhibit the phosphorylation of ß-catenin by the destruction complex. Dsh binds Axin and may help recruit its binding partner GBP to the destruction complex. GBP removes GSK3 from Axin, thereby disrupting the ability of GSK3 to phosphorylate ß-catenin. Unphosphorylated ß-catenin accumulates and enters the nucleus to activate the transcription of its target genes in a complex with TCF/LEF box transcription factors.